RGD Reference Report - Thiorphan, tiopronin, and related analogs as substrates and inhibitors of peptidylglycine alpha-amidating monooxygenase (PAM). - Rat Genome Database

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Thiorphan, tiopronin, and related analogs as substrates and inhibitors of peptidylglycine alpha-amidating monooxygenase (PAM).

Authors: McIntyre, NR  Lowe EW, JR  Chew, GH  Owen, TC  Merkler, DJ 
Citation: McIntyre NR, etal., FEBS Lett. 2006 Jan 23;580(2):521-32. Epub 2005 Dec 28.
RGD ID: 2302419
Pubmed: PMID:16405966   (View Abstract at PubMed)
DOI: DOI:10.1016/j.febslet.2005.12.058   (Journal Full-text)

Peptidyglycine alpha-amidating monooxygenase is a copper- and zinc-dependent, bifunctional enzyme that catalyzes the cleavage of glycine-extended peptides or N-acylglycines to the corresponding amides and glyoxylate. This reaction is a key step in the biosynthesis of bioactive alpha-amidated peptides and, perhaps, the primary fatty acids amides also. Two clinically useful N-acylglycines are thiorphan and tiopronin, each with a thiol moiety attached to the acyl group. We report here that thiorphan and tiopronin are substrates for PAM, exhibiting relatively low K(M,app) and V(MAX,app) values. The low V(MAX,app) values result, most likely, from a decrease in active PAM.2Cu(II) as the enzyme competes ineffectively with thiorphan and tiopronin for free copper.



Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
PamRatpeptidylamidoglycolate lyase activity  IDA  RGD 
PamRatpeptidylglycine monooxygenase activity  IDA  RGD 

Objects Annotated

Genes (Rattus norvegicus)
Pam  (peptidylglycine alpha-amidating monooxygenase)


Additional Information